Skip to content
Skip to main navigation
Skip to first column
Skip to second column
About SBS
News
Research News
Calendar
Directory
Associated Facilities
Organized Research Units
The Turtle Pond
Academics
Course Descriptions / Syllabi
Undergraduate Programs
Advising Center (BSAC)
Graduate Programs
Ecology, Evolution and Behavior
Microbiology
Plant Biology
Health Information Technologies
Student Views
Student Organizations
Alumni & Friends
Welcome
inVivo School Newsletter
Endowments
How to Give
Sections
Integrative Biology
Molecular Cell and Developmental Biology
Molecular Genetics and Microbiology
Neurobiology
SBS Directory
Faculty Profiles
Faculty & Staff Tools
Directory Update
CV Report
Biographical Sketch
TA Matching System
Academic Assignment
SBSPO
Room Reservations
New Employee Checklist
Grant Application Support
Online Store
Support Services
Text Book Order Forms
Contact Us
SBS Resources
Undergraduate Programs
Graduate Programs
Calendar
Directory
Maps
Online Store
Support Services
Contacts
UT resources
Job Resource Center
UT Direct
UT Directory
UT Calendars
Follow SBS
Home
»
Directory
» Details
Directory
Faculty
Austen Riggs
Professor Emeritus
Email:
riggs@uts.cc.utexas.edu
Website
Main Office:
PAT 506A
Phone:
471-1585
Alternate Office:
PAT 504-509
Alt. Phone:
471-7435
Mailing Address
The University of Texas at Austin - ICMB
1 University Station C0920
2415 Speedway
Austin ,TX 78712-0252
Research Summary
Interactions between and within macromolecular assemblages are frequently the key to understanding many complex cellular processes. I am particularly interested in the molecular mechanisms responsible for protein-protein interactions in hemoglobins. Current research concerns the structure, function and genetics of diverse hemoglobins that are widely distributed in all major groups of organisms including bacteria, fungi and higher plants as well as animals. We are studying the mechanisms by which self-association of subunits controls physiological function. The gigantic extracellular hemoglobin of the earthworm with over ~200 subunits is being studied as a model protein for understanding mechanisms by which calcium controls function. Collaborative studies of the two domain flavohemoglobin of yeast indicate that its function is as a nitric oxide dioxygenase. These studies utilize a combination of biophysical techniques and molecular biology. For example, site-directed-mutagenesis of lamprey hemoglobin together with ultracentrifugation, light scattering and measurement of oxygen binding has made possible the identification of the mechanisms responsible for the pH-dependent cooperative binding of oxygen. Biophysical techniques are now being applied to the assembly and function of the gigantic hemoglobin of the earthworm and its control by calcium.
Quick Links
About SBS
News
Research News
Calendar
Directory
Associated Facilities
Organized Research Units
The Turtle Pond